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PMR conformational studies of Pd(II) complexes with Ala-Tyr and D-Leu-Tyr dipeptides.
Autorzy
Rok wydania
1978
Czasopismo
Journal of Molecular Structure
Numer woluminu
50
Strony
73-80
DOI
10.1016/0022-2860(78)87098-7
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
PMR studies of Pd(II) complexes with Ala-Tyr and D-Leu-Tyr revealed the essential role of metal ion in inducing the dipeptide conformation in solution. In a complex with tridentate coordination of dipeptide (pH 3–10) the most stable conformer of a tyrosine residue is that with the aromatic ring in gauche position to carboxyl and amide groups. At high pH a dipeptide is a bidentate ligand (NH2, N−), the tyrosine residue changes its conformation drastically, and the most stable conformer is that with the aromatic ring in trans position to the carboxyl group. It was found that the C-terminal amino acid does not have any considerable influence on the conformation of an N-terminal amino acid in both kinds of complexes with palladium(II). Increasing the temperature up to 370 K has only a minor effect on the conformer population in solution.
Adres publiczny
https://doi.org/10.1016/0022-2860(78)87098-7
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